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full-length shp2 construct  (Novartis)

 
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    Structured Review

    Novartis full-length shp2 construct
    Allosteric regulation of <t>SHP2.</t> (A) The schematic representation of SHP2 structure and allosteric regulation. (B) The comparison of N-SH2 domain conformation at I (gray) and A (cyan) state. (C) The pY peptide binding surface in N-SH2 domain at I and A state. BG- and EF-loop are depicted in purple and yellow, respectively. (D) The N-SH2/PTP interaction surface in the N-SH2 domain at the I and A state.
    Full Length Shp2 Construct, supplied by Novartis, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/full-length shp2 construct/product/Novartis
    Average 90 stars, based on 1 article reviews
    full-length shp2 construct - by Bioz Stars, 2026-02
    90/100 stars

    Images

    1) Product Images from "Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases"

    Article Title: Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

    Journal: Chemical reviews

    doi: 10.1021/acs.chemrev.7b00105

    Allosteric regulation of SHP2. (A) The schematic representation of SHP2 structure and allosteric regulation. (B) The comparison of N-SH2 domain conformation at I (gray) and A (cyan) state. (C) The pY peptide binding surface in N-SH2 domain at I and A state. BG- and EF-loop are depicted in purple and yellow, respectively. (D) The N-SH2/PTP interaction surface in the N-SH2 domain at the I and A state.
    Figure Legend Snippet: Allosteric regulation of SHP2. (A) The schematic representation of SHP2 structure and allosteric regulation. (B) The comparison of N-SH2 domain conformation at I (gray) and A (cyan) state. (C) The pY peptide binding surface in N-SH2 domain at I and A state. BG- and EF-loop are depicted in purple and yellow, respectively. (D) The N-SH2/PTP interaction surface in the N-SH2 domain at the I and A state.

    Techniques Used: Comparison, Binding Assay

    Disease associated SHP2 mutations. (A) NS/cancer-associated SHP2 mutations mainly reside at the interface of N-SH2 and PTP domains. (B) LS-associated SHP2 mutations only appear within the PTP domain.
    Figure Legend Snippet: Disease associated SHP2 mutations. (A) NS/cancer-associated SHP2 mutations mainly reside at the interface of N-SH2 and PTP domains. (B) LS-associated SHP2 mutations only appear within the PTP domain.

    Techniques Used:

    LS SHP2 mutations reduce SHP2 phosphatase activity by disturbing different step(s) in the catalytic process. In this figure, SHP2 wild-type (gray) and mutant (green) were superimposed onto PTP1B (cyan) structure representing transition state 1 or 2 to show mutation-induced disturbance at each specific step. Residue numbers are shown in blue for PTP1B and black for SHP2. Red dash lines represent mutation induced steric conflicts.
    Figure Legend Snippet: LS SHP2 mutations reduce SHP2 phosphatase activity by disturbing different step(s) in the catalytic process. In this figure, SHP2 wild-type (gray) and mutant (green) were superimposed onto PTP1B (cyan) structure representing transition state 1 or 2 to show mutation-induced disturbance at each specific step. Residue numbers are shown in blue for PTP1B and black for SHP2. Red dash lines represent mutation induced steric conflicts.

    Techniques Used: Activity Assay, Mutagenesis, Residue

    The binding modes for two allosteric PTP inhibitors. (A) SHP099 binds at the inter-domain interfaces of SHP2 to stabilize the autoinhibited conformation. (B) Analog 3 binds at the trimer interfaces of PRL1 to prevent trimer formation.
    Figure Legend Snippet: The binding modes for two allosteric PTP inhibitors. (A) SHP099 binds at the inter-domain interfaces of SHP2 to stabilize the autoinhibited conformation. (B) Analog 3 binds at the trimer interfaces of PRL1 to prevent trimer formation.

    Techniques Used: Binding Assay



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    full-length shp2 construct  (Novartis)
    90
    Novartis full-length shp2 construct
    Allosteric regulation of <t>SHP2.</t> (A) The schematic representation of SHP2 structure and allosteric regulation. (B) The comparison of N-SH2 domain conformation at I (gray) and A (cyan) state. (C) The pY peptide binding surface in N-SH2 domain at I and A state. BG- and EF-loop are depicted in purple and yellow, respectively. (D) The N-SH2/PTP interaction surface in the N-SH2 domain at the I and A state.
    Full Length Shp2 Construct, supplied by Novartis, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/full-length shp2 construct/product/Novartis
    Average 90 stars, based on 1 article reviews
    full-length shp2 construct - by Bioz Stars, 2026-02
    90/100 stars
    		  Buy from Supplier
    the full-length shp2 construct  (Novartis)
    90
    Novartis the full-length shp2 construct
    Allosteric regulation of <t>SHP2.</t> (A) The schematic representation of SHP2 structure and allosteric regulation. (B) The comparison of N-SH2 domain conformation at I (gray) and A (cyan) state. (C) The pY peptide binding surface in N-SH2 domain at I and A state. BG- and EF-loop are depicted in purple and yellow, respectively. (D) The N-SH2/PTP interaction surface in the N-SH2 domain at the I and A state.
    The Full Length Shp2 Construct, supplied by Novartis, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/the full-length shp2 construct/product/Novartis
    Average 90 stars, based on 1 article reviews
    the full-length shp2 construct - by Bioz Stars, 2026-02
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Allosteric regulation of SHP2. (A) The schematic representation of SHP2 structure and allosteric regulation. (B) The comparison of N-SH2 domain conformation at I (gray) and A (cyan) state. (C) The pY peptide binding surface in N-SH2 domain at I and A state. BG- and EF-loop are depicted in purple and yellow, respectively. (D) The N-SH2/PTP interaction surface in the N-SH2 domain at the I and A state.

    Journal: Chemical reviews

    Article Title: Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

    doi: 10.1021/acs.chemrev.7b00105

    Figure Lengend Snippet: Allosteric regulation of SHP2. (A) The schematic representation of SHP2 structure and allosteric regulation. (B) The comparison of N-SH2 domain conformation at I (gray) and A (cyan) state. (C) The pY peptide binding surface in N-SH2 domain at I and A state. BG- and EF-loop are depicted in purple and yellow, respectively. (D) The N-SH2/PTP interaction surface in the N-SH2 domain at the I and A state.

    Article Snippet: 262 – 263 Utilizing the full-length SHP2 construct and screening for compounds that can block SHP2 activation by an N-SH2 domain binding pTyr peptide, the Novartis team identified several small molecule compounds that stabilize the auto-inhibited SHP2 conformation.

    Techniques: Comparison, Binding Assay

    Disease associated SHP2 mutations. (A) NS/cancer-associated SHP2 mutations mainly reside at the interface of N-SH2 and PTP domains. (B) LS-associated SHP2 mutations only appear within the PTP domain.

    Journal: Chemical reviews

    Article Title: Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

    doi: 10.1021/acs.chemrev.7b00105

    Figure Lengend Snippet: Disease associated SHP2 mutations. (A) NS/cancer-associated SHP2 mutations mainly reside at the interface of N-SH2 and PTP domains. (B) LS-associated SHP2 mutations only appear within the PTP domain.

    Article Snippet: 262 – 263 Utilizing the full-length SHP2 construct and screening for compounds that can block SHP2 activation by an N-SH2 domain binding pTyr peptide, the Novartis team identified several small molecule compounds that stabilize the auto-inhibited SHP2 conformation.

    Techniques:

    LS SHP2 mutations reduce SHP2 phosphatase activity by disturbing different step(s) in the catalytic process. In this figure, SHP2 wild-type (gray) and mutant (green) were superimposed onto PTP1B (cyan) structure representing transition state 1 or 2 to show mutation-induced disturbance at each specific step. Residue numbers are shown in blue for PTP1B and black for SHP2. Red dash lines represent mutation induced steric conflicts.

    Journal: Chemical reviews

    Article Title: Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

    doi: 10.1021/acs.chemrev.7b00105

    Figure Lengend Snippet: LS SHP2 mutations reduce SHP2 phosphatase activity by disturbing different step(s) in the catalytic process. In this figure, SHP2 wild-type (gray) and mutant (green) were superimposed onto PTP1B (cyan) structure representing transition state 1 or 2 to show mutation-induced disturbance at each specific step. Residue numbers are shown in blue for PTP1B and black for SHP2. Red dash lines represent mutation induced steric conflicts.

    Article Snippet: 262 – 263 Utilizing the full-length SHP2 construct and screening for compounds that can block SHP2 activation by an N-SH2 domain binding pTyr peptide, the Novartis team identified several small molecule compounds that stabilize the auto-inhibited SHP2 conformation.

    Techniques: Activity Assay, Mutagenesis, Residue

    The binding modes for two allosteric PTP inhibitors. (A) SHP099 binds at the inter-domain interfaces of SHP2 to stabilize the autoinhibited conformation. (B) Analog 3 binds at the trimer interfaces of PRL1 to prevent trimer formation.

    Journal: Chemical reviews

    Article Title: Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

    doi: 10.1021/acs.chemrev.7b00105

    Figure Lengend Snippet: The binding modes for two allosteric PTP inhibitors. (A) SHP099 binds at the inter-domain interfaces of SHP2 to stabilize the autoinhibited conformation. (B) Analog 3 binds at the trimer interfaces of PRL1 to prevent trimer formation.

    Article Snippet: 262 – 263 Utilizing the full-length SHP2 construct and screening for compounds that can block SHP2 activation by an N-SH2 domain binding pTyr peptide, the Novartis team identified several small molecule compounds that stabilize the auto-inhibited SHP2 conformation.

    Techniques: Binding Assay

    Allosteric regulation of SHP2. (A) The schematic representation of SHP2 structure and allosteric regulation. (B) The comparison of N-SH2 domain conformation at I (gray) and A (cyan) state. (C) The pY peptide binding surface in N-SH2 domain at I and A state. BG- and EF-loop are depicted in purple and yellow, respectively. (D) The N-SH2/PTP interaction surface in the N-SH2 domain at the I and A state.

    Journal: Chemical reviews

    Article Title: Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

    doi: 10.1021/acs.chemrev.7b00105

    Figure Lengend Snippet: Allosteric regulation of SHP2. (A) The schematic representation of SHP2 structure and allosteric regulation. (B) The comparison of N-SH2 domain conformation at I (gray) and A (cyan) state. (C) The pY peptide binding surface in N-SH2 domain at I and A state. BG- and EF-loop are depicted in purple and yellow, respectively. (D) The N-SH2/PTP interaction surface in the N-SH2 domain at the I and A state.

    Article Snippet: 262 – 263 Utilizing the full-length SHP2 construct and screening for compounds that can block SHP2 activation by an N-SH2 domain binding pTyr peptide, the Novartis team identified several small molecule compounds that stabilize the auto-inhibited SHP2 conformation.

    Techniques: Binding Assay

    Disease associated SHP2 mutations. (A) NS/cancer-associated SHP2 mutations mainly reside at the interface of N-SH2 and PTP domains. (B) LS-associated SHP2 mutations only appear within the PTP domain.

    Journal: Chemical reviews

    Article Title: Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

    doi: 10.1021/acs.chemrev.7b00105

    Figure Lengend Snippet: Disease associated SHP2 mutations. (A) NS/cancer-associated SHP2 mutations mainly reside at the interface of N-SH2 and PTP domains. (B) LS-associated SHP2 mutations only appear within the PTP domain.

    Article Snippet: 262 – 263 Utilizing the full-length SHP2 construct and screening for compounds that can block SHP2 activation by an N-SH2 domain binding pTyr peptide, the Novartis team identified several small molecule compounds that stabilize the auto-inhibited SHP2 conformation.

    Techniques:

    LS SHP2 mutations reduce SHP2 phosphatase activity by disturbing different step(s) in the catalytic process. In this figure, SHP2 wild-type (gray) and mutant (green) were superimposed onto PTP1B (cyan) structure representing transition state 1 or 2 to show mutation-induced disturbance at each specific step. Residue numbers are shown in blue for PTP1B and black for SHP2. Red dash lines represent mutation induced steric conflicts.

    Journal: Chemical reviews

    Article Title: Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

    doi: 10.1021/acs.chemrev.7b00105

    Figure Lengend Snippet: LS SHP2 mutations reduce SHP2 phosphatase activity by disturbing different step(s) in the catalytic process. In this figure, SHP2 wild-type (gray) and mutant (green) were superimposed onto PTP1B (cyan) structure representing transition state 1 or 2 to show mutation-induced disturbance at each specific step. Residue numbers are shown in blue for PTP1B and black for SHP2. Red dash lines represent mutation induced steric conflicts.

    Article Snippet: 262 – 263 Utilizing the full-length SHP2 construct and screening for compounds that can block SHP2 activation by an N-SH2 domain binding pTyr peptide, the Novartis team identified several small molecule compounds that stabilize the auto-inhibited SHP2 conformation.

    Techniques: Activity Assay, Mutagenesis

    The binding modes for two allosteric PTP inhibitors. (A) SHP099 binds at the inter-domain interfaces of SHP2 to stabilize the autoinhibited conformation. (B) Analog 3 binds at the trimer interfaces of PRL1 to prevent trimer formation.

    Journal: Chemical reviews

    Article Title: Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

    doi: 10.1021/acs.chemrev.7b00105

    Figure Lengend Snippet: The binding modes for two allosteric PTP inhibitors. (A) SHP099 binds at the inter-domain interfaces of SHP2 to stabilize the autoinhibited conformation. (B) Analog 3 binds at the trimer interfaces of PRL1 to prevent trimer formation.

    Article Snippet: 262 – 263 Utilizing the full-length SHP2 construct and screening for compounds that can block SHP2 activation by an N-SH2 domain binding pTyr peptide, the Novartis team identified several small molecule compounds that stabilize the auto-inhibited SHP2 conformation.

    Techniques: Binding Assay